UniProt: A0A023B8W0

Database: UniProt
Entry: A0A023B8W0_GRENI

LinkDB:  A0A023B8W0_GRENI 
Original site:  A0A023B8W0_GRENI

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (23)   

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ID   A0A023B8W0_GRENI        Unreviewed;      1801 AA.
AC   A0A023B8W0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=GNI_055600 {ECO:0000313|EMBL:EZG70485.1};
OS   Gregarina niphandrodes (Septate eugregarine).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC   Eugregarinorida; Gregarinidae; Gregarina.
OX   NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG70485.1, ECO:0000313|Proteomes:UP000019763};
RN   [1] {ECO:0000313|EMBL:EZG70485.1, ECO:0000313|Proteomes:UP000019763}
RP   NUCLEOTIDE SEQUENCE.
RA   Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA   Brunk B., Roos D., Caler E., Lorenzi H.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EZG70485.1}.
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DR   EMBL; AFNH02000422; EZG70485.1; -; Genomic_DNA.
DR   RefSeq; XP_011129936.1; XM_011131634.1.
DR   EnsemblProtists; EZG70485; EZG70485; GNI_055600.
DR   GeneID; 22912058; -.
DR   VEuPathDB; CryptoDB:GNI_055600; -.
DR   eggNOG; KOG0968; Eukaryota.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000019763; Unassembled WGS sequence.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019763};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          713..815
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          886..1197
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          1411..1449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1611..1648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1716..1746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1429..1445
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1731..1746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1801 AA;  201158 MW;  94CA6D08462B2416 CRC64;
     MLGFRPVTID CVYSHTFKPG LGDTLTNAIS GLQVYTCSQI VMTGTTLVCA SNRSQDRVPE
     SQLPGSQGLS EDVLGWNPSV KAGPESVVYV HGFKPIMYFR IEKFLVDAAL SQLGECSCGQ
     CDQLTVVCVR CSGDNLNTLP LTSDHNCCRV CKFTNALIEA GIRHHPDMSR EIHQVKMAEK
     RTKRSLALIY NVQLVAKRPL YGYHLNSSLF AQISCCQPYD PPRIGSMIIQ GLFGGIPLQC
     YELHISAVVR FMRMCGIAGP EWLYFQRRNC FLRSSNKECV NNVFEFDINM AHLINVTAGT
     HTATKLVDGP SAVGTTCTDG CNLVDLCKEA DRNFVWDVRQ IENTVQKWSA DMSLLDSPWE
     SYRNTEIDVM DTMPRYCQED LSRIVQAIER AHTCVRPDEI EETGAKSNAG PVETTAILLS
     QVHFDNSQPF ATEVPKPYST NPDCLKQKNP YAYRYLKGCP IGHIERCAAG RTGDELPMVG
     RNYVYFIPPP DKELLMNELL VLKKNGIIKC SDPEDALLLS APLASAPTQN FEPPVSTSPK
     SSVYQKIDKV TTKSPAHKRF GRLLYVEPVL NICPPVDRGS DGVPCLVDGS SVDMPNAEGE
     TEDIALRQIA CLKRDRGIPE IDQVTCIVLS WEEYLIGGDA SKPTGTVLLY LDGSEGTTGG
     KEWTGENATG GSQGCKEDTE ADHIIRSFPP SSRNPYMTPG TPEAQQLLPN CLCNVQILSN
     EIDLISTAFK FIRLIDPTII VGWDNKFYGI GYLWARYKFL TGDPACTLQV SRFTNTTFNL
     PVDAARAKLS SKICKIGGRT YLNGGKLCRE DTKLNDVSFL NMVKCTLGLI LPRMELHVLS
     LYWHTGGRRA FVIRMIMNRV EAFRRMLWKQ GVIGKYVSLS SVFYVEWSAS ITRGSQFFVE
     AIMLSACRNL GCILSSLSKQ QVRDQDALEA IPMVLEPKSK CYTCPVIVVD YQSLYPSLMI
     AYNICYSTCI GKAHRVYQAI NQYLQNPNTD FGNIRIGGVD VALNMKEIVH ALAQDPKSFH
     VLPNGVMFCN KSIREGVLPV IMRSVLASRI FVKRAMSRGK KRLSSEVLSL MNFSQQSLKF
     VSVTTYGYIG ASVTGRMPCG DIADGIVSSG RHLLDCTMHW IEAQDFGRPI EVVYGDTDSC
     FIHVPGSSMP EAFNIGQQVC AMIVRKTLHP LTLKLEKVYE SCVLQTKKRY VGHAYETLDD
     WLSERIVLPR LPSASPSEIM EKRLYKLLTL GPIRYGLKGF FDSKGVEASR RDQSDLIQIA
     VSRILKSMFY WRDLAQVQRE FKKIVLEIGK ATTKNVITQL DDIKPFSGRI VDSEAAFGYP
     KDWLQYGRAS HGKTLSFKGR ETRHIWPRDF IAIKRLKLGH YSYHGTNKAH TLPPQAVVAL
     WCQNILRSGL PMLKKLNTKY EPFAKGRNHF NFRGNAERTT GPREDGVNSE GDQDDEGTDE
     QEEPPEEQGF MYHTGEGFGY VIAAGSGTLN SLAALPSRCV STPFFPLGRE HVWSAVTHRW
     YLSLNNLQLN EEYYRRVVTA TVSRMLDLLD PLPPSAAFQW LKSMHHVNRA EGLSAEPLGL
     CTFAALDPFS LPSTQLLFWG LRGHERRTLG RDQRTLGHEQ GEQIVVEVDR PATIDEATDR
     NTTTTDSTRT NAPERRHDGP HLRTRRRPAP YNAVLKGVTL GVYVTAKKTT QTPPVPQPPP
     LTLGGQVDDW KRCQRPTAVS IHPQTRSLVM TDGADLRDLD EPEPDPAEAD QPTSTKPTST
     KPTSASLKEH VFLHDAQSKL VMCRRLCLMC TGGCLEDVEN CVDAYHCPVY SMRTNLSRIM
     R
//

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